| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna28030.1-v1.0-hybrid |
| Family | CE10 |
| Protein Properties | Length: 477 Molecular Weight: 52388 Isoelectric Point: 8.4448 |
| Chromosome | Chromosome/Scaffold: 6 Start: 37602930 End: 37605695 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 162 | 451 | 0 |
| RGYSPANSAKKSRKLPVILQFHGGGWVSGSNDSVANDCFCRRIAKLCDVIVVAVGYRLAPENRYPAAFEDGLKVLNWLGKQANLANLSMGGATELKKTDN RHIVDTFGASMVEPWLAAHGDPSRCVLLGVSCGANIADYVARKAVEAGKLLEPVKVVAQVLMYPFFVGSVPTHSEIKLANSYFYDKAMCMLAWKLFLPEE EFSLDHPAANPLIPDRQPPLKLMPPTLTVVAEHDWMRDRAIAYSEELRKVNVDAPVMEYKDAVHEFATLDMLLKTPQAQACAEDIAIWKL | |||
| Full Sequence |
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| Protein Sequence Length: 477 Download |
| MPSVAVKLYS VFFKFLLKHR LQNRIQTRPD DFDPFGVTSR PEETIAAANP LFDDDGVATK 60 DIHIDPFTSL SIRIFLPESA LSPPEPSVKS RPRRPDLNSP SVSDSARPSP NGSPFHSSRR 120 NSYGNAAAAN TLKAEPRRSS YGFSNDVEGL NLMAGVGAGV YRGYSPANSA KKSRKLPVIL 180 QFHGGGWVSG SNDSVANDCF CRRIAKLCDV IVVAVGYRLA PENRYPAAFE DGLKVLNWLG 240 KQANLANLSM GGATELKKTD NRHIVDTFGA SMVEPWLAAH GDPSRCVLLG VSCGANIADY 300 VARKAVEAGK LLEPVKVVAQ VLMYPFFVGS VPTHSEIKLA NSYFYDKAMC MLAWKLFLPE 360 EEFSLDHPAA NPLIPDRQPP LKLMPPTLTV VAEHDWMRDR AIAYSEELRK VNVDAPVMEY 420 KDAVHEFATL DMLLKTPQAQ ACAEDIAIWK LSKENSSLLL LPGAYTAKSF RWPLPR* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00135 | COesterase | 1.0e-6 | 164 | 300 | 152 | + Carboxylesterase family. | ||
| cd00312 | Esterase_lipase | 6.0e-7 | 164 | 295 | 141 | + Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. | ||
| PRK10162 | PRK10162 | 4.0e-7 | 162 | 252 | 96 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 2.0e-34 | 161 | 447 | 287 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 3.0e-62 | 179 | 428 | 250 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2zsi_A | 2e-33 | 176 | 430 | 113 | 331 | A Chain A, Structure Of Fructose-Bisphosphate Aldolase |
| PDB | 2zsh_A | 2e-33 | 176 | 430 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 3e-31 | 176 | 430 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 3e-31 | 176 | 430 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 3e-31 | 176 | 430 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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